3.4.24.17: stromelysin 1
This is an abbreviated version!
For detailed information about stromelysin 1, go to the full flat file.
Word Map on EC 3.4.24.17
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3.4.24.17
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metalloproteinases
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mmp-1
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cartilage
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arthritis
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joint
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osteoarthritis
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rheumatoid
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synovial
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chondrocytes
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necrosis
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timps
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articular
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gelatinase
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tnf
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interleukin-1
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knee
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zymography
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degeneration
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aggrecan
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proteoglycans
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c-reactive
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interstitial
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gelatin
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plasminogen
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proteinases
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cox-2
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synoviocytes
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il-1beta
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fibroblast-like
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cruciate
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intervertebral
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ligament
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matrilysin
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pulposus
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matrix-degrading
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adamts-4
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synovitis
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thrombospondin
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intra-articular
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subchondral
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emmprin
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chondroprotective
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photoaging
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collagenases
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diagnostics
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medicine
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aggrecanase
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prommp-9
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neoepitope
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gelatinolytic
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mt1-mmp
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collagenolytic
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drug development
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analysis
- 3.4.24.17
- metalloproteinases
- mmp-1
- cartilage
- arthritis
- joint
- osteoarthritis
-
rheumatoid
- synovial
- chondrocytes
- necrosis
- timps
-
articular
- gelatinase
- tnf
- interleukin-1
- knee
-
zymography
- degeneration
- aggrecan
- proteoglycans
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c-reactive
-
interstitial
- gelatin
- plasminogen
- proteinases
- cox-2
- synoviocytes
- il-1beta
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fibroblast-like
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cruciate
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intervertebral
- ligament
- matrilysin
- pulposus
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matrix-degrading
- adamts-4
- synovitis
- thrombospondin
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intra-articular
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subchondral
-
emmprin
-
chondroprotective
-
photoaging
- collagenases
- diagnostics
- medicine
- aggrecanase
-
prommp-9
-
neoepitope
-
gelatinolytic
- mt1-mmp
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collagenolytic
- drug development
- analysis
Reaction
preferential cleavage where P1', P2' and P3' are hydrophobic residues =
Synonyms
Collagen-activating protein, Collagenase activating protein, matrix metalloprotease-3, Matrix metalloproteinase 3, matrix metalloproteinase-3, matrixin, MMP-3, MMP3, Neutral proteoglycanase, Procollagenase activator, Proteoglycanase, PTR1 protein, ST1, Stromelysin, stromelysin-1, Transin
ECTree
3.4.24.17 stromelysin 1Advanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.17 - stromelysin 1
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
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hydrolyzed 60 times more rapidly by metalloproteinase-3 than metalloproteinase-1, little discrimination between metalloproteinase-3 and metalloproteinase-2
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-
?
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu + norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
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-
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?
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
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a fluorogenic substrate selectively hydrolyzed by stromelysin 1
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-
?
(7-methoxycoumarin-4-yl)acetyl-P-L-G-L-(L)-2,3-diaminopropionylamide-A-R + H2O
?
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-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
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-
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?
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly + H2O
?
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hydrolyzed equally well by metalloproteinase-3 and metalloproteinase-2, metalloproteinase-1 shows 25% of the activity compared to metalloproteinase-3
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-
?
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala-norvaline-Trp-NH2 + H2O
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala + norvaline-Trp-NH2
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-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
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-
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?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
6-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hexanoy-L-Arg-L-Pro-L-Lys-L-Pro-L-Leu-L-Ala-L-Nva-L-Trp-L-Lys(7-dimethylaminocoumarin-4-yl)-NH2 + H2O
?
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?
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 + H2O
?
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?
Antithrombin III + H2O
?
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cleavage of the P1-P1' bond in the reactive center
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-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
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fluorogenic substrate
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-
?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
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-
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?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
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-
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?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
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alpha1-proteinase inhibitor, cleavage within the reactive site loop
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?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
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?
cytosolic protein Apaf-1 + H2O
?
the 130 kD full-length Apaf-1 is truncated to about 37 kD and 20 kD proteins
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?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
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?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
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-
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?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
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?
Laminin + H2O
?
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cleavage activity is barely detected as a much lower activity as reported
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?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
activation
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-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
an additional cytosolic protein, possibly Apaf-1, is required for activation, rat substrate
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?
Collagen type IV + H2O
additional information
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4 major fragments of MW 165000, 145000, 125000 and 110000
?
Collagen type IV + H2O
additional information
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no degradation of type I collagen
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-
?
Collagen type IV + H2O
additional information
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limited activity
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?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
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?
additional information
?
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degrades a number of extracellular matrix components
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-
?
additional information
?
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participates in activation of procollagenases and progelatinase B
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?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
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?
additional information
?
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degrades a number of extracellular matrix components
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-
?
additional information
?
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participates in activation of procollagenases and progelatinase B
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?
additional information
?
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may play a role in the normal turnover of the connective tissue matrix as well as in the joint destruction of chronic synovitis
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?
additional information
?
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believed to play a role in pathological conditions such as arthritis and tumor invasion
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?
additional information
?
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degrading all of the major macromolecules of the extracellular matrix
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?
additional information
?
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required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling
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?
additional information
?
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stromelysin (MMP3), through its action on collagen and other matrix metalloproteinases, influences arterial wall remodeling
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-
?
additional information
?
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matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
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-
?
additional information
?
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the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
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?
additional information
?
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the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
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?
additional information
?
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the enzyme degrades several dentin matrix proteins, a demineralized and pretreated dentin block is used for activity assays. Enzyme MMP-3 is capable of degrading the protein core of proteoglycans, resulting in the release of soluble glycosaminoglycans
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?
additional information
?
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enzyme attacks the basal lamina and tight junction proteins, opening the blood-brain barrier and thereby facilitating neutrophil influx
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?
additional information
?
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enzyme is expressed as a protective response and plays an important role in host defense during squamous cell carcinoma tumorigenesis
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?
additional information
?
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genetic ablation of MMP-3 does not significantly affect tumor growth and metastasis in the MMTV-PyMT model
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?
additional information
?
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MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
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?
additional information
?
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degradation of glomerular basement membrane
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?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
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?
additional information
?
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degrades a number of extracellular matrix components
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?
additional information
?
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participates in activation of procollagenases and progelatinase B
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-
?
additional information
?
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cleavage at multiple chondroitin sulfate-binding sites along the protein core
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?
additional information
?
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glomerular basement membrane degradation by glomeruli may be attributable to stromelysin and suggest an important role for these proteinases in glomerular pathophysiology
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?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
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?
additional information
?
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degrades a number of extracellular matrix components
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-
?
additional information
?
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participates in activation of procollagenases and progelatinase B
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?
Proteoglycan + H2O
additional information
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cartilage
degradation to 12.0 S fragments by the HMW form and 10.3 S fragments by the KMW enzyme
?
